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3S46

The crystal structure of alanine racemase from streptococcus pneumoniae

Replaces:  3MUB
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0006522biological_processalanine metabolic process
A0008784molecular_functionalanine racemase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016853molecular_functionisomerase activity
A0030170molecular_functionpyridoxal phosphate binding
A0030632biological_processD-alanine biosynthetic process
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0006522biological_processalanine metabolic process
B0008784molecular_functionalanine racemase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016853molecular_functionisomerase activity
B0030170molecular_functionpyridoxal phosphate binding
B0030632biological_processD-alanine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BEZ A 369
ChainResidue
AHIS28
AILE29
APRO30
BGLU141
BALA142
BARG183
BTHR186
BHOH393
BHOH453

Functional Information from PROSITE/UniProt
site_idPS00395
Number of Residues11
DetailsALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANAYGHG
ChainResidueDetails
AALA37-GLY47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201
ChainResidueDetails
ALLP40
BLLP40

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201
ChainResidueDetails
ATYR263
BTYR263

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01201
ChainResidueDetails
AARG136
AMET310
BARG136
BMET310

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALLP40
BLLP40

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000269|PubMed:21612658
ChainResidueDetails
AKCX129
BKCX129

218853

PDB entries from 2024-04-24

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